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Ligand phenylmethanesulfonyl fluoride

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Basic Ligand Information

Molecular Structure
Picture of phenylmethanesulfonyl fluoride (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C7H7FO2S
phenylmethanesulfonyl fluoride
YBYRMVIVWMBXKQ-UHFFFAOYSA-N
Synonyms:
(phenylmethyl)sulfonyl fluoride, C6H5CH2SO3F, p-methylsulfonylfluoride, phenyl-methanesulfonyl fluoride, phenyl-methyl-sulfonyl-fluoride, phenylmethane-sulfonylfluoride, phenylmethanesulfonly fluoride, phenylmethanesulfonylflouride, Phenylmethanesulfonylfluoride, phenylmethane sulfonyl fluoride, phenylmethane sulfonylfluoride, phenyl methane sulfonyl fluoride, Phenylmethanesulphonyl fluoride, phenylmethanosulfonyl fluorate, Phenylmethyl-sulfonyl fluoride, phenylmethylsufonyl fluoride, phenylmethylsulfonic fluoride, phenylmethylsulfonyl-fluoride, phenylmethylsulfonyl fluoride, phenyl methylsulfonyl fluoride, phenyl methyl sulfonylfluoride, phenyl methyl sulfonyl fluoride, phenyl methylsulfonylfluoride, Phenylmethyl sulfonylfluoride, phenylmethyl sulfonyl fluoride, Phenylmethylsulfonylfluoride, Phenylmethylsulphonylfluoride, Phenylmethylsulphonyl fluoride, phenyl methyl sulphonyl fluoride, PMSF

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
glutaryl-CoA + phenylmethylsulfonyl fluoride = ?
show the reaction diagram
-
phenylmethylsulfonyl fluoride + H2O = ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
111% activity at 1 mM
-
2 mM, 167% of initial activity
-
exposure of the enzyme to phenylmethylsulfonyl fluoride results in the LAAO expressing anticoagulant activity, preventing contact activation generated thrombin from forming a clot
-
slightly activating
-
1 mM + 1 mM DTT, activation to 147% of control
-
80 mM, relative activity 114%
-
0.1 mM: inhibition of intracellular proteolytic proteins during the incubation of disrupted yeast cells for RNA hydrolysis
-
0.1 mM, 63% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
0.1 mM, 63% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
activates 14% at 5 mM
-
5 mM, 28% increase in enzyme activity
-
113.77% activity at 5 mM
-
activates xylanase I, inhibits xylanase II
-
5 mM, 1.1fold activation
-
activates 14% at 5 mM
-
activates
-
weak activation
-
5 mM, 1.2fold activation
-
slight activation at 1 mM
-
123% activity at 0.5 mM
-
slight activation at 1 mM
-
1 mM, 40% inhibition
-
1 mm, 126% of initial activity
-

Inhibitor in Enzyme-catalyzed Reactions (917 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
63% inhibition at 10 mM
-
about 10% inhibition at 1 mM
-
lower molecular weight form
-
85% inhibition at 5 mM
-
about 48% inhibition at 5 mM
-
1 mM, 30% inhibition, incubation for 1 min
-
0.5 mM 50% inhibition of cytosolic form, little effect on chloroplastic form
-
weak inhibition
-
5 mM, 49% residual activity
-
uncompetitive inhibition, 50% inhibition
-
decreases the enzyme activity by about 18% at 2 mM
-
20 mM, 59% residual activity
-
61% activity at 1 mM
-
0.2 mM, inhibits the 8R-dioxygenase enzyme by over 85%
-
79.9% residual activity at 5 mM
-
strong inhibitor
-
inactivates NPADH, presumably by modifying the active site cysteine
-
non-competitive
-
60% residual activity at 1 mM with feruloyl-CoA as substrate
-
slight inhibition
-
about 20% inhibition of isoform LAAOII and about 90% inhibition of isoform LAAOI at 5 mM
-
31.8% residual activity at 10 mM
-
0.1 mM, 93% inhibition
-
i.e. PMSF, chloroplast enzyme, slight inhibition
-
1 mM, 36.8% residual activity
-
58% inhibition
-
complete inhibition at 10 mM
-
complete inhibition at 5 mM
-
30% inhibition at 50 mM
-
treatment of purified SlCGT with 1, 10, and 50 mM PMSF leads to strong decreases in caffeoyl transfer activities to 60%, 40%, and 0% activity, respectively
-
slight inhibition at 1 mM
-
70.88% residual activity at 1 mM
-
strong inhibition at 10 mM
-
1 mM, 65% irreversible inhibition, 1.5 M ATP protect
-
inhibits 65% at 5 mM
-
about 25% residual activity at 1 mM
-
almost complete inhibition
-
1 mM
-
1 mM, 54% inhibition
-
1 mM, 15% of initial activity; 1 mM, 55% of initial activity; 1 mM, 60% of initial activity
-
50% inhibition at about 8 mM PMSF
-
75% inhibition at 1 mM
-
20% inhibition at 1 mM
-
1 mM, 26.4% inhibition, Phedase type 2; 1 mM, 61% inhibition, Phedase type 1
-
1 mM, complete inhibition
-
10.5% residual activity after 10 min of incubation with 2 mM
-
50 mM, 100% inhibition
-
strong inhibition of 4-nitrophenylacetate hydrolysis
-
inhibition of wild-type YeiG and YeiG mutants C54A and C26A
-
FS-44: 5'-PDase activity of bifunctional enzyme: cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase
-
70.3% residual activity at 2 mM
-
2 mM, 94% inhibition
-
21.2% inhibition at 2 mM
-
5 mM, 60% inhibition
-
23% residual activity in the presence of 5 mM phenylmethylsulfonyl fluoride, after 30 min at 30°C
-
about 2% residual activity at 1% (v/v)
-
78% inhibition at 5 mM
-
47.5% inhibition at 1 mM
-
no inhibition of isozyme MG4, 47% inhibition of isozyme MG6
-
35.54% residual activity at 10 mM
-
partially
-
about 35% residual activity at 1 mM
-
10 mM, activity decreases by about 50%
-
1 mM, 4°C, 10 h incubation, 76% inhibition
-
81.4% residual activity at 10 mM
-
9% inhibition at 5 mM
-
80.3% residual activity at 5 mM
-
strong inhibitor, after preincubation of the purified enzyme for 1 h at 0°C
-
5 mM, inhibition to 75% of control
-
about 60% residual activity at 1 mM; about 65% residual activity at 10 mM
-
27% inhibition at 1 mM at pH 7.4
-
6 mM 29% inhibition; 6 mM, 29% inhibition
-
1 mM, 40% inhibition; 1 mM, 64% inhibition
-
70.04% residual activity at 10 mM
-
41% inhibition at 1 mM
-
88.5% inhibition at 1 mM
-
less than 40% residual activity at 1 mM
-
1 mM, no residual activity
-
weak
-
0.1 mM and 1 mM, 78.1% and 21.4% compared to a control without additives
-
0.1 mM, proPoCtX: 42.2% inhibition, native PoCtX: 37.2% inhibition
-
weak
-
2 mM, 15% inhibition
-
10 mM, 21% inhibition
-
80% inhibition at 1 mM
-
51% inhibition at 5 mM
-
12% inhibition at 0.05 mM
-
1 mM, 42% inhibition of amidolytic activity
-
2 mM, complete inhibition
-
complete inhibition
-
partial inhibition
-
50% loss of activtity
-
0.6 mM, 50% inhibition
-
at high concentrations
-
almost complete inhibition at 10 mM
-
20 mM
-
80% ihibition
-
1 mM, 87% inhibition
-
5 mM, 21% inhibition
-
1 mM, 87% inhibition
-
weak inhibition
-
53.68% inhibition at 0.1 mM
-
13.22% inhibition at 0.1 mM
-
1 mM, 6% inhibition
-
incubation with 100 mM phenylmethylsulfonyl fluoride for 30 min decreases activity to 63% of the initial value, but inhibition is partially reverted when 12 mM cysteine is added to the reaction mixture
-
complete inhibition
-
3 mM, 16% inhibition
-
PMSF does not affect activity when using 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) as a substrate. With 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp), PMSF shows no effect on truncated protease and 30% inhibition of full-length NSP2
-
16.3% residual activity at 5 mM
-
complete inhibition at 10 mM
-
weak inhibitor
-
slight
-
weak inhibition
-
weak
-
2 mM, 36.4% inhibition
-
strongly inhibited, 100% inhibition
-
50% inhibition at 1 mM
-
PMSF, 80% inhibition at 1 mM
-
1 mM, 68% inhibition after 1 h
-
slight inhibition
-
1 mM, 45% inhibition
-
10 mM: 9.8% activity; strong inhibition
-
31% inhibition at 1 mM, complete inhibition at 10 mM
-
2 mM, 10% inhibition
-
weak
-
weak
-
1 mM, 77% loss of activity
-
strong inhibition, 0.1 mM: 95% inhibition, 0.01 mM: 84% inhibition
-
1 mM, 80% inhibition
-
5 mM, 31% inhibition
-
irreversible inhibition
-
15% inhibition at 1 mM
-
1 mM, 64% loss of activity
-
NG,NG-dimethyl-L-arginine release from freeze-thaw whole blood 57% inhibited
-
1 mM, dextran-conjugated enzyme and native enzyme retain 1.1% and 1.2% of their initial activities
-
1 mM, 51% inhibition
-
about 10% residual activity at 1% (w/v)
-
1 mM, 71.7% residual activity
-
10 mM: 63% of maximal activity
-
83% reduced activity at 1 mM
-
1 mM, 7.6% inhibition
-
2 mM, 33% inhibition
-
10 mM, 59% inhibition
-
52.3% residual activity at 10 mM
-
59% inhibition at 1 mM
-
partial inhibition at 0.1 mM, complete inhibition at 1 mM
-
1 mM, strong inhibition
-
1 mM, strong inhibition
-

Metals and Ions (4 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates 12% at 1 mM
-
activation of isozymes A and B
-
activates chymotrypsin-like activity
-

3D Structure of Enzyme-Ligand-Complex (PDB) (3 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (1 result)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
16
-
-

Ki Value (3 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.15
-
-
0.1
-
-
0.6
-
-

IC50 Value (16 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.2
-
at pH 7.4 and 37°C
0.24
-
mediocre inhibitor, IC50: 0.24 mM
0.6
-
IC50: 0.6 mM
0.63
-
pH 7.5, 21°C, recombinant enzyme

References & Links

Links to other databases for phenylmethanesulfonyl fluoride

EXTERNAL LINKS